ID   HSP83_DROAV             Reviewed;         716 AA.
AC   O02192;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Heat shock protein 83;
DE   AltName: Full=HSP 82;
GN   Name=Hsp83; Synonyms=Hsp82;
OS   Drosophila auraria (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=47315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=3040.11B;
RX   PubMed=9493358; DOI=10.1007/pl00006310;
RA   Konstantopoulou I., Scouras Z.G.;
RT   "The heat-shock gene hsp83 of Drosophila auraria: genomic organization,
RT   nucleotide sequence, and long antiparallel coupled ORFs (LAC ORFs).";
RL   J. Mol. Evol. 46:334-343(1998).
CC   -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC       maintenance and proper regulation of specific target proteins involved
CC       for instance in cell cycle control and signal transduction. Undergoes a
CC       functional cycle that is linked to its ATPase activity. This cycle
CC       probably induces conformational changes in the client proteins, thereby
CC       causing their activation. Interacts dynamically with various co-
CC       chaperones that modulate its substrate recognition, ATPase cycle and
CC       chaperone function. Required for piRNA biogenesis by facilitating
CC       loading of piRNAs into PIWI proteins (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with shu (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC       repeat-containing proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; U75687; AAB58358.1; -; Genomic_DNA.
DR   AlphaFoldDB; O02192; -.
DR   SMR; O02192; -.
DR   PRIDE; O02192; -.
DR   FlyBase; FBgn0020208; Daur\Hsp83.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..716
FT                   /note="Heat shock protein 83"
FT                   /id="PRO_0000062929"
FT   REGION          213..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           712..716
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        226..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   716 AA;  81760 MW;  9EC59F027C4DFCD7 CRC64;
     MPEEAETFAF QAEIAQLMSL IINTFYSNKE IFLRELISNA SDALDKIRYE SLTDPSKLDS
     GKELYIKLIP NKTAGTLTII DTGIGMTKSD LVNNLGTIAK SGTKAFMEAL QAGADISMIG
     QFGVGFYSAY LVADKVTVTS KNNDDEQYIW ESSAGGSFTV RADNSEPLGR GTKIVLYIKE
     DQTDYLEESK IKEIVNKHSQ FIGYPIKLLV EKEREKEVSD DEADDDKKED EKKEMDTDEP
     KIEDVGEDED ADKKDKDAKK KKTIKEKYTE DEELNKTKPI WTRNPDDISQ EEYGEFYKSL
     TNDWEDHLAV KHFSVEGQLE FRALLFIPRR TPFDLFENQK KRNNIKLYVR RVFIMDNCED
     LIPEYLNFIK GVVDSEDLPL NISREMLQQN KVLKVIRKNL VKKTMELIEE LTEDKENYKK
     FYDQFSKNLK LGVHEDSNNR AKLADFLRFH TSASGDDFCS LSDYVSRMKE NQKHVYFITG
     ESKDQVSNSA FVERVKARGF EVVYMTEPID EYVIQHLKEY KGKQLVSVTK EGLELPEDDA
     EKKKREEDKA KFESLCKLMN AILDNKVEKV VVSNRLVDSP CCIVTSQFGW SANMERIMKA
     QALRDTATMG YMAGKKQLEI NPDHPIVETL RQKADADKND KAVKDLVILL FETSLLSSGF
     SLDSPQVHAS RIYRMIKLGL GIDEDEPMTT EDAQSAGDAP SLVEDTEDAS HMEEVD